CitMHS family explained
The Citrate-Mg2+:H+ (CitM) / Citrate-Ca2+:H+ (CitH) Symporter (CitMHS) Family (TC# 2.A.11) is a family of transport proteins belonging to the Ion transporter superfamily.[1] Members of this family are found in Gram-positive and Gram-negative bacteria, archaea and possibly eukaryotes. These proteins all probably arose by an internal gene duplication event. Lensbouer & Doyle (2010) have reviewed these systems, classifying the porters with three superfamilies, according to ion-preference:[2]
1) Mg2+-preferring,
2) Ca2+-preferring, and
3) Fe2+-preferring.
A representative list of proteins belonging to the CitMHS family can be found in the Transporter Classification Database.[3]
CitM and CitH
Two of the characterized members of the CitMHS family, both citrate uptake permeases from Bacillus subtilis, are CitM (TC# 2.A.11.1.1) and CitH (TC# 2.A.11.1.2).
Function
CitM is believed to transport a citrate2−-Mg2+complex in symport with one H+ per Mg2+-citrate while CitH apparently transports a citrate2−-Ca2+ complex in symport with protons.[4] [5] The cation specificity of CitM is: Mg2+, Mn2+, Ba2+, Ni2+, Co2+, Ca2+ and Zn2+, in this preferential order. CitM is highly specific for citrate and D-isocitrate and does not transport other di- and tri-carboxylates including succinate, L-isocitrate, cis-aconitate and tricarballylate.[6] [7] For CitH, the cation specificity (in order of preference) is: Ca2+, Ba2+ and Sr2+. The two proteins are 60% identical, contain about 400 amino acyl residues and possess twelve putative transmembrane spanners. A CitM homologue in S. mutans transports citrate conjugated to Fe2+ or Mn2+ but not Ca2+, Mg2+ or Ni2+.[8]
The transport reactions catalyzed by (1) CitM and (2) CitH, respectively, are:
(1) Citrate • Mg (out) + nH+ (out) ⇌ Citrate • Mg (in) + nH+ (in)
(2) Citrate (out) + nH+ (out) ⇌ Citrate (in) + nH+ (in)
(3) Citrate • Ca2+ (out) + nH+ (out) ⇌ Citrate • Ca2+ (in) + nH+ (in)
See also
Notes and References
- Prakash. Shraddha. Cooper. Garret. Singhi. Soumya. Saier. Milton H.. 2003-12-03. The ion transporter superfamily. Biochimica et Biophysica Acta (BBA) - Biomembranes. 1618. 1. 79–92. 0006-3002. 14643936. 10.1016/j.bbamem.2003.10.010.
- Lensbouer. Joshua J.. Patel. Ami. Sirianni. Joseph P.. Doyle. Robert P.. 2008-08-01. Functional characterization and metal ion specificity of the metal-citrate complex transporter from Streptomyces coelicolor. Journal of Bacteriology. 190. 16. 5616–5623. 10.1128/JB.00456-08. 1098-5530. 2519374. 18556792.
- Web site: 2.A.11. The Citrate-Mg2+:H+ (CitM) Citrate-Ca2+:H+ (CitH) Symporter (CitMHS) Family. Transporter Classification Database. 2016-03-04.
- Boorsma. A.. van der Rest. M. E.. Lolkema. J. S.. Konings. W. N.. 1996-11-01. Secondary transporters for citrate and the Mg(2+)-citrate complex in Bacillus subtilis are homologous proteins. Journal of Bacteriology. 178. 21. 6216–6222. 0021-9193. 178492. 8892821. 10.1128/jb.178.21.6216-6222.1996.
- Krom. B. P.. Warner. J. B.. Konings. W. N.. Lolkema. J. S.. 2000-11-01. Complementary metal ion specificity of the metal-citrate transporters CitM and CitH of Bacillus subtilis. Journal of Bacteriology. 182. 22. 6374–6381. 0021-9193. 94783. 11053381. 10.1128/jb.182.22.6374-6381.2000.
- Li. H.. Pajor. A. M.. 2002-01-01. Functional characterization of CitM, the Mg2+-citrate transporter. The Journal of Membrane Biology. 185. 1. 9–16. 10.1007/s00232-001-0106-1. 0022-2631. 11891560. 8677932.
- Warner. Jessica B.. Lolkema. Juke S.. 2002-11-01. Growth of Bacillus subtilis on citrate and isocitrate is supported by the Mg2+-citrate transporter CitM. Microbiology. 148. Pt 11. 3405–3412. 10.1099/00221287-148-11-3405. 1350-0872. 12427932. free.
- Korithoski. Bryan. Krastel. Kirsten. Cvitkovitch. Dennis G.. 2005-07-01. Transport and metabolism of citrate by Streptococcus mutans. Journal of Bacteriology. 187. 13. 4451–4456. 10.1128/JB.187.13.4451-4456.2005. 0021-9193. 1151779. 15968054.